Q5NDE7
Gene name |
pomgnt2 (ago61, gtdc2) |
Protein name |
Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 |
Names |
POMGnT2, Extracellular O-linked N-acetylglucosamine transferase-like, Glycosyltransferase-like domain-containing protein 2 |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:444520 |
EC number |
2.4.1.312: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5NDE7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5NDE7-F1 | Predicted | AlphaFoldDB |
No variants for Q5NDE7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5NDE7 | |||||
No associated diseases with Q5NDE7
1 regional properties for Q5NDE7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Fibronectin type III | 484 - 578 | IPR003961 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.312 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetylglucosaminyltransferase activity | Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| neuron migration | The characteristic movement of an immature neuron from germinal zones to specific positions where they will reside as they mature. |
| protein O-linked glycosylation | A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan. |
| protein O-linked mannosylation | The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNISAVFSAL | LVSIMAAVLW | KHVKLLDQFY | VIEEELELTR | QSQELSQVRI | DYQAALQALV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EDGTRMVCSG | RMHTDRVCRF | ESLCYSTEAE | EFVFFHSNAS | IMLPNLGPRR | FQPALLDLSS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VDDHNTQYFN | FIELPAAALK | FMPKPVFVPD | VALIMNRFNP | DNLMHVFHDD | LLPIFYTIQQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FPDLDFESRL | FFMEGWNEGL | HFELYKFMSN | KQPLLKEQLK | TLGRLLCFTK | SYVGLSKITT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| WYQYGFVQPQ | GPKANILVSG | NEIRHFAKFM | MGKLNITLDQ | NAAEAYIVLF | SRSMNRLIVN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EAELLLALAQ | EFQMKTITVS | LEDHSFSDIV | RLLSNATMLV | SMHGAQLVTS | LFLPKGAVVV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ELFPYGINPE | HYTPYKTLST | LPGMELQYVA | WQNTEEENTI | TYPDRPWEQG | GIVHLETKEQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ERIKKSKEVP | RHLCCRNPEW | LFRIYQDTKV | NISSLIQVIK | STVKKKLGLR | RQKWTQGLYP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GKVRESKCQA | SAQGTSEAKL | FVSWQIPWNL | KFLKVRDVKY | EVWIQEQGEN | SYMPYILSQQ |
| 550 | 560 | 570 | |||
| NYTFSENIKP | FTTYLVWIRC | IFNKTLLGPF | AEVLVCST |